{PDOC00136}
{PS00150; ACYLPHOSPHATASE_1}
{PS00151; ACYLPHOSPHATASE_2}
{PS51160; ACYLPHOSPHATASE_3}
{BEGIN}
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* Acylphosphatase-like domain signatures and profile *
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Acylphosphatase (EC  3.6.1.7)  [1,2]  catalyzes the hydrolysis of various acyl
phosphate carboxyl-phosphate   bonds  such  as  carbamyl  phosphate,  succinyl
phosphate, 1,3-diphosphoglycerate, etc.  The physiological role of this enzyme
is not yet clear.  Acylphosphatase is a small protein of around 100 amino-acid
residues. Two  different isoenzymes are expressed in mammalian tissues: muscle
type (MT)  acylphosphatase  is  prevalently  found  in the skeletal muscle and
heart, whereas  the  organ  common  type  (CT) acylphosphatase is expressed in
erythrocytes, brain and testis.

While acylphosphatase  have  been  so  far  only characterized in vertebrates,
there are  a number of bacterial and archebacterial hypothetical proteins that
are highly similar to that enzyme and that probably possess the same activity.
These proteins are:

 - Escherichia coli probable acylphosphatase yccX.
 - Bacillus subtilis probable acylphosphatase yflL.
 - Archaeoglobus fulgidus probable acylphosphatase AF0818.

An acylphosphatase-like  domain is also found in the N-terminus of prokaryotic
hydrogenase maturation protein hypF [3,4].

The acylphosphatase-like  domain  forms  a compact, pear-shaped, stucture (see
<PDB:2ACY>). It  has  a  globular  alpha/beta fold, consisting of a beta sheet
with five  antiparallel  strands  and two alpha helices packed parallel on the
same side   of   the  sheet,  forming  an  alpha/beta  sandwich  protein.  The
acylphosphatase-like domain  is  stabilized  by intramolecular contacts of the
two antiparallel   amphipatic  alpha-helices,  which  pack  their  hydrophobic
residues against the inner face of the beta-sheet, leaving no core cavities in
the proteins structure [4,5].

As signature patterns, we selected two conserved regions. The first is located
in the  N-terminal  section,  while the second is found in the central part of
the protein  sequence.  We  also  developed  a  profile that covers the entire
acylphosphatase-like domain.

-Consensus pattern: [LIV]-x-G-x-V-Q-[GH]-V-x-[FM]-R
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: G-[FYW]-[AVC]-[KRQAM]-N-x(3)-G-x-V-x(5)-G
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Stefani M., Ramponi G.
     "Acylphosphate phosphohydrolases."
     Life Chem. Rep. 12:271-301(1995).
[ 2] Stefani M., Taddei N., Ramponi G.
     "Insights into acylphosphatase structure and catalytic mechanism."
     Cell. Mol. Life Sci. 53:141-151(1997).
     PubMed=9118002
[ 3] Wolf I., Buhrke T., Dernedde J., Pohlmann A., Friedrich B.
     "Duplication of hyp genes involved in maturation of [NiFe]
     hydrogenases in Alcaligenes eutrophus H16."
     Arch. Microbiol. 170:451-459(1998).
     PubMed=9799289
[ 4] Rosano C., Zuccotti S., Bucciantini M., Stefani M., Ramponi G.,
     Bolognesi M.
     "Crystal structure and anion binding in the prokaryotic hydrogenase
     maturation factor HypF acylphosphatase-like domain."
     J. Mol. Biol. 321:785-796(2002).
     PubMed=12206761
[ 5] Thunnissen M.M.G.M., Taddei N., Liguri G., Ramponi G., Nordlund P.
     "Crystal structure of common type acylphosphatase from bovine
     testis."
     Structure 5:69-79(1997).
     PubMed=9016712

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